TY - JOUR
T1 - Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor κB-mediated transactivations
AU - Na, Soon Young
AU - Lee, Soo Kyung
AU - Han, Su Ji
AU - Choi, Hueng Sik
AU - Im, Suhn Young
AU - Lee, Jae Woon
PY - 1998/5/1
Y1 - 1998/5/1
N2 - Steroid receptor coactivator-1 (SRC-1) specifically bound to the transcription factor NFκB subunit p50 but not to p65 as demonstrated by the yeast two hybrid tests and glutathione S-transferase pull down assays. The p50-binding site was localized to a subregion of SRC-1 (amino acids 759- 1141) that encompasses the previously described CBP-p300-binding domain. In mammalian cells, SRC-1 potentiated the NFκB-mediated transactivations in a dose-dependent manner. Coexpression of p300 further enhanced this SRC-1- potentiated level of transactivations, consistent with the recent findings in which CBP and p300 were shown to be transcription coactivators of the p65 subunit (Perkins, N. D., Felzien, L. K., Betts, J. C., Leung, K., Beach, D. H., and Nabel, G. J. (1997) Science 275, 523-527; Gerritsen, M. E., Williams, A. J., Neish, A- S., Moore, S., Shi, Y., and Collins, T. (1997) Proc. Acad. Natl. Sci. U. S. A. 94, 2927-2932). These results suggest that at least two distinct coactivator molecules may cooperate to regulate the NFκB-dependent transactivations in vive and SRC-1, originally identified as a coactivator for the nuclear receptors, may constitute a more widely used coactivation complex.
AB - Steroid receptor coactivator-1 (SRC-1) specifically bound to the transcription factor NFκB subunit p50 but not to p65 as demonstrated by the yeast two hybrid tests and glutathione S-transferase pull down assays. The p50-binding site was localized to a subregion of SRC-1 (amino acids 759- 1141) that encompasses the previously described CBP-p300-binding domain. In mammalian cells, SRC-1 potentiated the NFκB-mediated transactivations in a dose-dependent manner. Coexpression of p300 further enhanced this SRC-1- potentiated level of transactivations, consistent with the recent findings in which CBP and p300 were shown to be transcription coactivators of the p65 subunit (Perkins, N. D., Felzien, L. K., Betts, J. C., Leung, K., Beach, D. H., and Nabel, G. J. (1997) Science 275, 523-527; Gerritsen, M. E., Williams, A. J., Neish, A- S., Moore, S., Shi, Y., and Collins, T. (1997) Proc. Acad. Natl. Sci. U. S. A. 94, 2927-2932). These results suggest that at least two distinct coactivator molecules may cooperate to regulate the NFκB-dependent transactivations in vive and SRC-1, originally identified as a coactivator for the nuclear receptors, may constitute a more widely used coactivation complex.
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U2 - 10.1074/jbc.273.18.10831
DO - 10.1074/jbc.273.18.10831
M3 - Article
C2 - 9556555
AN - SCOPUS:0032080237
SN - 0021-9258
VL - 273
SP - 10831
EP - 10834
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 18
ER -